2au3

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[[Image:2au3.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of the Aquifex aeolicus primase (Zinc Binding and RNA Polymerase Domains)==
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|PDB= 2au3 |SIZE=350|CAPTION= <scene name='initialview01'>2au3</scene>, resolution 2.00&Aring;
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<StructureSection load='2au3' size='340' side='right'caption='[[2au3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[2au3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AU3 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE= dnaG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2au3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2au3 OCA], [https://pdbe.org/2au3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2au3 RCSB], [https://www.ebi.ac.uk/pdbsum/2au3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2au3 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2au3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2au3 OCA], [http://www.ebi.ac.uk/pdbsum/2au3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2au3 RCSB]</span>
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== Function ==
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[https://www.uniprot.org/uniprot/DNAG_AQUAE DNAG_AQUAE] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/2au3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2au3 ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of the Aquifex aeolicus primase (Zinc Binding and RNA Polymerase Domains)'''
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==See Also==
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*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The coordination of primase function within the replisome is an essential but poorly understood feature of lagging strand synthesis. By using crystallography and small-angle X-ray scattering (SAXS), we show that functional elements of bacterial primase transition between two dominant conformations: an extended form that uncouples a regulatory domain from its associated RNA polymerase core and a compact state that sequesters the regulatory region from the site of primer synthesis. FRET studies and priming assays reveal that the regulatory domain of one primase subunit productively associates with nucleic acid that is bound to the polymerase domain of a second protomer in trans. This intersubunit interaction allows primase to select initiation sites on template DNA and implicates the regulatory domain as a "molecular brake" that restricts primer length. Our data suggest that the replisome may cooperatively use multiple primases and this conformational switch to control initiation frequency, processivity, and ultimately, Okazaki fragment synthesis.
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==About this Structure==
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2AU3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AU3 OCA].
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==Reference==
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Crosstalk between primase subunits can act to regulate primer synthesis in trans., Corn JE, Pease PJ, Hura GL, Berger JM, Mol Cell. 2005 Nov 11;20(3):391-401. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16285921 16285921]
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[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Berger, J M.]]
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[[Category: Berger JM]]
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[[Category: Corn, J E.]]
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[[Category: Corn JE]]
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[[Category: Hura, G L.]]
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[[Category: Hura GL]]
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[[Category: Pease, P J.]]
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[[Category: Pease PJ]]
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[[Category: dna replication]]
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[[Category: rna polymerase]]
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[[Category: toprim]]
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[[Category: zinc ribbon]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:57:20 2008''
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Current revision

Crystal Structure of the Aquifex aeolicus primase (Zinc Binding and RNA Polymerase Domains)

PDB ID 2au3

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